We describe the modification of reactive actin sulfhydryls by S-nitrosoglutathione. Kinetics of S-nitrosylation and denitrosylation suggest that only one cysteine of actin is involved in the reactions. By using the bifunctional sulfhydryl cross-linking reagent N,N'-1,4- phenylenebismaleimide and the monofunctional reagent N-iodoacetyl-N'-(5- sulpho-1-naphthyl)ethylenediamine, we identified this residue as Cys374. The time course of filament formation followed by high-shear viscosity changes revealed that S-nitrosylated G-actin polymerizes less efficiently than native monomers. The observed decrease in specific viscosity at steady state is due mainly to a marked inhibition of filament end-to-end annealing and, partially, to a reduction in F-actin concentration. Finally, S-nitrosylated actin acts as nitric oxide donor showing a fast, potent vasodilating activity at unusually low concentrations, being comparable with that of low molecular weight nitrosothiols.
DALLE DONNE, I., Milzani, A., Giustarini, D., DI SIMPLICIO, P., Colombo, R., Rossi, R. (2000). S-NO-actin: S-nitrosylation kinetics and the effect on isolated vascular smooth muscle. JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY, 21(2), 171-181 [10.1023/A:1005671319604].
S-NO-actin: S-nitrosylation kinetics and the effect on isolated vascular smooth muscle
GIUSTARINI D;DI SIMPLICIO P.;ROSSI, RANIERI
2000-01-01
Abstract
We describe the modification of reactive actin sulfhydryls by S-nitrosoglutathione. Kinetics of S-nitrosylation and denitrosylation suggest that only one cysteine of actin is involved in the reactions. By using the bifunctional sulfhydryl cross-linking reagent N,N'-1,4- phenylenebismaleimide and the monofunctional reagent N-iodoacetyl-N'-(5- sulpho-1-naphthyl)ethylenediamine, we identified this residue as Cys374. The time course of filament formation followed by high-shear viscosity changes revealed that S-nitrosylated G-actin polymerizes less efficiently than native monomers. The observed decrease in specific viscosity at steady state is due mainly to a marked inhibition of filament end-to-end annealing and, partially, to a reduction in F-actin concentration. Finally, S-nitrosylated actin acts as nitric oxide donor showing a fast, potent vasodilating activity at unusually low concentrations, being comparable with that of low molecular weight nitrosothiols.File | Dimensione | Formato | |
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https://hdl.handle.net/11365/410542